ID   KUNI_ORNMO              Reviewed;         119 AA.
AC   P56409;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ornithodorin {ECO:0000303|PubMed:8947023};
DE   AltName: Full=Thrombin inhibitor {ECO:0000303|PubMed:8947023};
OS   Ornithodoros moubata (Soft tick) (Argasid tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodoros.
OX   NCBI_TaxID=6938;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH THROMBIN, RECOMBINANT
RP   EXPRESSION, AND DISULFIDE BONDS.
RX   PubMed=8947023;
RA   van de Locht A., Stubbs M.T., Bode W., Friedrich T., Bollschweiler C.,
RA   Hoffken W., Huber R.;
RT   "The ornithodorin-thrombin crystal structure, a key to the TAP enigma?";
RL   EMBO J. 15:6011-6017(1996).
CC   -!- FUNCTION: Tick salivary thrombin inhibitor that plays an important part
CC       in the anti-hemostatic strategy of ticks (Probable). Is a potent and
CC       highly selective thrombin inhibitor (Ki=10 pM) (PubMed:8947023).
CC       {ECO:0000269|PubMed:8947023, ECO:0000305|PubMed:8947023}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:Q8MVZ2}. Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000305|PubMed:8947023}.
CC   -!- DOMAIN: Has two domains of the BPTI family. The N-terminal domain bind
CC       to the active site of thrombin, the C-terminal domain binds at the
CC       fibrinogen recognition exosite. {ECO:0000305|PubMed:8947023}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PDB; 1TOC; X-ray; 3.10 A; R/S/T/U=1-119.
DR   PDBsum; 1TOC; -.
DR   AlphaFoldDB; P56409; -.
DR   SMR; P56409; -.
DR   MEROPS; I02.024; -.
DR   MEROPS; I02.032; -.
DR   EvolutionaryTrace; P56409; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.410.10; -; 2.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   SUPFAM; SSF57362; SSF57362; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation cascade inhibiting toxin;
KW   Cytoplasmic vesicle; Disulfide bond; Hemostasis impairing toxin;
KW   Protease inhibitor; Repeat; Secreted; Serine protease inhibitor; Toxin.
FT   CHAIN           1..119
FT                   /note="Ornithodorin"
FT                   /id="PRO_0000155458"
FT   DOMAIN          1..53
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT                   ECO:0000305|PubMed:8947023"
FT   DOMAIN          61..116
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000305|PubMed:8947023"
FT   REGION          54..60
FT                   /note="Linker"
FT   DISULFID        5..50
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   DISULFID        13..35
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   DISULFID        29..46
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   DISULFID        65..113
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   DISULFID        73..96
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   DISULFID        89..109
FT                   /evidence="ECO:0000269|PubMed:8947023,
FT                   ECO:0007744|PDB:1TOC"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   HELIX           43..49
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   TURN            84..87
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          88..96
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:1TOC"
FT   HELIX           106..112
FT                   /evidence="ECO:0007829|PDB:1TOC"
SQ   SEQUENCE   119 AA;  12632 MW;  3A595D2C76D63235 CRC64;
     LNVLCNNPHT ADCNNDAQVD RYFREGTTCL MSPACTSEGY ASQHECQQAC FVGGEDHSSE
     MHSSCLGDPP TSCAEGTDIT YYDSDSKTCK VLAASCPSGE NTFESEVECQ VACGAPIEG